Enzymatic and non-enzymatic functions of secreted phospholipases A2

Authors

  • Anna Król Chair of Environmental Chemistry and Bioanalytics, Faculty of Chemistry, Nicolaus Copernicus University, Toruń, Poland
  • Maciej Ostrowski Department of Biochemistry, Faculty of Biology and Environmental Protection, Nicolaus Copenicus University, Toruń, Poland

Abstract

Phospholipases catalyze enzymatic degradation of membrane lipids. The phospholipases are divided into four major groups: A1, A2, C, and D by the type of ester bond which is hydrolyzed. Phospholipases A2 (PLA2) hydrolyze membrane glycerophospholipids at sn-2 position releasing lysophospholipid and free fatty acid. The PLA2s are involved in biosynthesis of intracellular messengers (eicosanoids), endo- and exocytosis, and cytoskeleton reorganization. Moreover, secreted PLA2 play various functions which are not dependent on their enzymatic activity. An intriguing question is specific interaction of sPLA2
from snake venom with several protein acceptors (human coagulation factor Xa or CFTR). In this review, we describe classification of PLA, mechanism of catalytic action, as well as interactions of snake venom PLA2 with various human proteins.

Downloads

Download data is not yet available.

Published

2018-02-15

Issue

Section

Articles